NHAP2_SALG2
ID NHAP2_SALG2 Reviewed; 577 AA.
AC B5R8Z9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=K(+)/H(+) antiporter NhaP2 {ECO:0000255|HAMAP-Rule:MF_01075};
DE AltName: Full=Potassium/proton antiporter NhaP2 {ECO:0000255|HAMAP-Rule:MF_01075};
GN Name=nhaP2 {ECO:0000255|HAMAP-Rule:MF_01075}; Synonyms=cvrA;
GN OrderedLocusNames=SG1315;
OS Salmonella gallinarum (strain 287/91 / NCTC 13346).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=550538;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=287/91 / NCTC 13346;
RX PubMed=18583645; DOI=10.1101/gr.077404.108;
RA Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S.,
RA Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A.,
RA Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B.,
RA Ormond D., Abdellah Z., Brooks K., Cherevach I., Chillingworth T.,
RA Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S.,
RA Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., Maskell D.,
RA Humphreys T., Roberts M., Barrow P.A., Dougan G., Parkhill J.;
RT "Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella
RT gallinarum 287/91 provides insights into evolutionary and host adaptation
RT pathways.";
RL Genome Res. 18:1624-1637(2008).
CC -!- FUNCTION: K(+)/H(+) antiporter that extrudes potassium in exchange for
CC external protons and maintains the internal concentration of potassium
CC under toxic levels. {ECO:0000255|HAMAP-Rule:MF_01075}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(out) + K(+)(in) = H(+)(in) + K(+)(out);
CC Xref=Rhea:RHEA:29467, ChEBI:CHEBI:15378, ChEBI:CHEBI:29103;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01075};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29468;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01075};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01075}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01075}.
CC -!- SIMILARITY: Belongs to the monovalent cation:proton antiporter 1 (CPA1)
CC transporter (TC 2.A.36) family. NhaP2 subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_01075}.
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DR EMBL; AM933173; CAR37192.1; -; Genomic_DNA.
DR RefSeq; WP_000338368.1; NC_011274.1.
DR AlphaFoldDB; B5R8Z9; -.
DR SMR; B5R8Z9; -.
DR EnsemblBacteria; CAR37192; CAR37192; SG1315.
DR KEGG; seg:SG1315; -.
DR HOGENOM; CLU_005912_9_2_6; -.
DR OMA; QIGMFVL; -.
DR Proteomes; UP000008321; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0015386; F:potassium:proton antiporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006884; P:cell volume homeostasis; IEA:InterPro.
DR Gene3D; 1.20.1530.20; -; 1.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.1450; -; 1.
DR HAMAP; MF_01075; NhaP2; 1.
DR InterPro; IPR006153; Cation/H_exchanger.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR038770; Na+/solute_symporter_sf.
DR InterPro; IPR030151; NhaP.
DR InterPro; IPR023729; NhaP2.
DR InterPro; IPR006037; RCK_C.
DR InterPro; IPR036721; RCK_C_sf.
DR InterPro; IPR005170; Transptr-assoc_dom.
DR PANTHER; PTHR32507:SF7; PTHR32507:SF7; 1.
DR Pfam; PF03471; CorC_HlyC; 1.
DR Pfam; PF00999; Na_H_Exchanger; 1.
DR Pfam; PF02080; TrkA_C; 1.
DR SMART; SM01091; CorC_HlyC; 1.
DR SUPFAM; SSF116726; SSF116726; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR PROSITE; PS51202; RCK_C; 1.
PE 3: Inferred from homology;
KW Antiport; Cell inner membrane; Cell membrane; Ion transport; Membrane;
KW Potassium; Potassium transport; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..577
FT /note="K(+)/H(+) antiporter NhaP2"
FT /id="PRO_1000136712"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
FT TRANSMEM 334..354
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
FT TRANSMEM 363..383
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
FT DOMAIN 403..485
FT /note="RCK C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01075"
SQ SEQUENCE 577 AA; 62451 MW; 5E6AECDFBD7EEC1A CRC64;
MDAATIISLF ILGSILVTSS ILLSSFSSRL GIPILVIFLA IGMLAGVDGI GGIPFDNYPF
AYIVSNLALA IILLDGGMRT QASSFRVALG PALSLATLGV LITSGLTGMM AAWLFHLDLI
EGLLIGAIVG STDAAAVFSL LGGKGLNERV GSTLEIESGS NDPMAVFLTI TLIEMIQKHE
TGLDWMFAVH IIQQFGLGIV FGLGGGYLLQ QMINRISLPS GLYPMLALSG GILIFALTTA
LEGSGILAVY LCGFLLGNRP IRNRYGILQN FDGLAWLAQI AMFLVLGLLV TPSDLWPIAV
PALILSIWMI FFARPLSVFT GLLPFRGFNL RERIFISWVG LRGAVPIILA VFPMMAGLEN
ARLFFNVAFF VVLVSLLLQG TSLSWAAKRA KVVVPPVGWP VSRVGLDIHP DNPWEQFIYQ
LSADKWCVGA ALRDLHMPNE TRIAALFRNN ELFHPTGSTR LQEGDVLCVI GRERDLPALG
KLFSQSPPVS LDQRFFGDFI LEANAKFADV ALIYGLEEGT EYRDKQQTLG EIIQQLLGAA
PVVGDQVEFG GMIWTVAEKE DNVVRKIGVR VAEDEAE
